Evidence map›Paper›PMID 24391950›Full record

ArticlePloS one2013

Flotillins directly interact with γ-catenin and regulate epithelial cell-cell adhesion.

Nina Kurrle, Frauke Völlner, Rüdiger Eming, Michael Hertl, Antje Banning, Ritva Tikkanen

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.0field-weighted citation impact, top 16% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

16 citing papers in PubMed, 33 citations in OpenAlex.

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  5. Flotillins: At the Intersection of ProteinInternational journal of molecular sciences · 2020
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Nina KurrleInstitute of Biochemistry, Medical Faculty, Justus Liebig University, Giessen, Germany.
Frauke VöllnerInstitute of Biochemistry, Medical Faculty, Justus Liebig University, Giessen, Germany.
Rüdiger EmingDepartment of Dermatology and Allergology, Phillips University, Marburg, Germany.
Michael HertlDepartment of Dermatology and Allergology, Phillips University, Marburg, Germany.
Antje BanningInstitute of Biochemistry, Medical Faculty, Justus Liebig University, Giessen, Germany.
Ritva TikkanenInstitute of Biochemistry, Medical Faculty, Justus Liebig University, Giessen, Germany.
University of Giessen · DEPhilipps University of Marburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Flotillin-1 and flotillin-2 are two homologous, membrane raft associated proteins. Although it has been reported that flotillins are involved in cell adhesion processes and play a role during breast cancer progression, thus making them interesting future therapeutic targets, their precise function has not been well elucidated. The present study investigates the function of these proteins in cell-cell adhesion in non-malignant cells. We have used the non-malignant epithelial MCF10A cells to study the interaction network of flotillins within cell-cell adhesion complexes. RNA interference was used to examine the effect of flotillins on the structure of adherens junctions and on the association of core proteins, such as E-cadherin, with membrane rafts. We here show that the cadherin proteins of the adherens junction associate with flotillin-2 in MCF10A cells and in various human cell lines. In vitro, flotillin-1 and flotillin-2 directly interact with γ-catenin which is so far the only protein known to be present both in the adherens junction and the desmosome. Mapping of the interaction domain within the γ-catenin sequence identified the Armadillo domains 6-8, especially ARM domain 7, to be important for the association with flotillins. Furthermore, depletion of flotillins significantly influenced the morphology of the adherens junction in human epithelial MCF10A cells and altered the association of E-cadherin and γ-catenin with membrane rafts. Taken together, these observations suggest a functional role for flotillins, especially flotillin-2, in cell-cell adhesion in non-malignant epithelial cells.

Indexed as

Adherens JunctionsAnalysis of VarianceBlotting, WesternCadherinsCell AdhesionCell LineDNA PrimersEpithelial CellsFluorescent Antibody Techniquegamma CateninHumansImmunoprecipitationMembrane ProteinsPlasmidsRNA InterferenceCadherinsDNA Primersflotillinsgamma CateninMembrane Proteins

Identifiers

PMID24391950
PMCPMC3877284
OpenAlexW1985878598

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.